ID   PDXK_STAES              Reviewed;         276 AA.
AC   Q8CTQ7;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Putative pyridoxine kinase;
DE            EC=2.7.1.35;
DE   AltName: Full=PN/PL/PM kinase;
DE   AltName: Full=Pyridoxal kinase;
DE   AltName: Full=Pyridoxamine kinase;
DE   AltName: Full=Vitamin B6 kinase;
GN   Name=pdxK; OrderedLocusNames=SE_0349;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Phosphorylates B6 vitamers; functions in a salvage pathway.
CC       Uses pyridoxal, pyridoxine, and pyridoxamine as substrates (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC         Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC         EC=2.7.1.35;
CC   -!- SIMILARITY: Belongs to the ThiD family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO03946.1; -; Genomic_DNA.
DR   RefSeq; NP_763904.1; NC_004461.1.
DR   RefSeq; WP_002458379.1; NZ_WBME01000045.1.
DR   AlphaFoldDB; Q8CTQ7; -.
DR   SMR; Q8CTQ7; -.
DR   STRING; 176280.SE_0349; -.
DR   EnsemblBacteria; AAO03946; AAO03946; SE_0349.
DR   GeneID; 50019488; -.
DR   KEGG; sep:SE_0349; -.
DR   PATRIC; fig|176280.10.peg.323; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_0_9; -.
DR   OMA; KDEVGYA; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR045029; HMP/HMP-P_kinase.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR20858; PTHR20858; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..276
FT                   /note="Putative pyridoxine kinase"
FT                   /id="PRO_0000192033"
FT   BINDING         139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         176..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  29845 MW;  E14B714B794331A7 CRC64;
     MALKKVLTIA GSDTSAGAGM QADLKTFQEL DVYGMVALTS IVTMDKETWS HDVTPIDMNV
     FEKQLETAIS IGPDAIKTGM LGTQDIIKRA GDVFVESGAD YFVVDPVMVC KGEDEVLNPG
     NTEAMIQYLL PKATVVTPNL FEAGQLSGLG KLTSIEDMKK AAQVIYDKGT PHVIIKGGKA
     LDQDKSYDLY YDGQQFYQLT TDMFQQSYNH GAGCTFAAAT TAYLANGKSP KEAIIAAKAF
     VASAIKNGWK MNDFVGPVDH GAYNRIEQIN VEVTEV